This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1szc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1szc.png|left|200px]]
 
- 
-
<!--
 
-
The line below this paragraph, containing "STRUCTURE_1szc", creates the "Structure Box" on the page.
 
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
 
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
 
-
or leave the SCENE parameter empty for the default display.
 
-
-->
 
{{STRUCTURE_1szc| PDB=1szc | SCENE= }}
{{STRUCTURE_1szc| PDB=1szc | SCENE= }}
- 
===Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD+-dependent Sir2 histone/protein deacetylases===
===Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD+-dependent Sir2 histone/protein deacetylases===
 +
{{ABSTRACT_PUBMED_15150415}}
-
 
+
==Function==
-
<!--
+
[[http://www.uniprot.org/uniprot/HST2_YEAST HST2_YEAST]] NAD-dependent histone deacetylase that is involved in nuclear silencing events. Derepresses subtelomeric silencing and increases repression in nucleolar (rDNA) silencing. Its function is negatively regulated by active nuclear export.<ref>PMID:10811920</ref> <ref>PMID:11106374</ref> <ref>PMID:11226170</ref> <ref>PMID:15274642</ref> <ref>PMID:17110954</ref>
-
The line below this paragraph, {{ABSTRACT_PUBMED_15150415}}, adds the Publication Abstract to the page
+
-
(as it appears on PubMed at http://www.pubmed.gov), where 15150415 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_15150415}}
+
==About this Structure==
==About this Structure==
Line 22: Line 10:
==Reference==
==Reference==
-
<ref group="xtra">PMID:015150415</ref><ref group="xtra">PMID:014502267</ref><ref group="xtra">PMID:014604530</ref><references group="xtra"/>
+
<ref group="xtra">PMID:015150415</ref><references group="xtra"/><references/>
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Chai, X.]]
[[Category: Chai, X.]]

Revision as of 08:47, 23 April 2014

Template:STRUCTURE 1szc

Contents

Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD+-dependent Sir2 histone/protein deacetylases

Template:ABSTRACT PUBMED 15150415

Function

[HST2_YEAST] NAD-dependent histone deacetylase that is involved in nuclear silencing events. Derepresses subtelomeric silencing and increases repression in nucleolar (rDNA) silencing. Its function is negatively regulated by active nuclear export.[1] [2] [3] [4] [5]

About this Structure

1szc is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

  • Zhao K, Harshaw R, Chai X, Marmorstein R. Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases. Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8563-8. Epub 2004 May 18. PMID:15150415 doi:10.1073/pnas.0401057101
  1. Landry J, Sutton A, Tafrov ST, Heller RC, Stebbins J, Pillus L, Sternglanz R. The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc Natl Acad Sci U S A. 2000 May 23;97(11):5807-11. PMID:10811920 doi:http://dx.doi.org/10.1073/pnas.110148297
  2. Tanner KG, Landry J, Sternglanz R, Denu JM. Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14178-82. PMID:11106374 doi:http://dx.doi.org/10.1073/pnas.250422697
  3. Perrod S, Cockell MM, Laroche T, Renauld H, Ducrest AL, Bonnard C, Gasser SM. A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast. EMBO J. 2001 Jan 15;20(1-2):197-209. PMID:11226170 doi:http://dx.doi.org/10.1093/emboj/20.1.197
  4. Borra MT, Langer MR, Slama JT, Denu JM. Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases. Biochemistry. 2004 Aug 3;43(30):9877-87. PMID:15274642 doi:http://dx.doi.org/10.1021/bi049592e
  5. Wilson JM, Le VQ, Zimmerman C, Marmorstein R, Pillus L. Nuclear export modulates the cytoplasmic Sir2 homologue Hst2. EMBO Rep. 2006 Dec;7(12):1247-51. Epub 2006 Nov 17. PMID:17110954 doi:http://dx.doi.org/10.1038/sj.embor.7400829

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools